PP2A and Aurora differentially modify Cdc13 to promote telomerase release from telomeres at G2/M phase

Zih-Jie Shen, Pang-Hung Hsu, Yu-Tai Su, Chia-Wei Yang, Li Kao, Shun-Fu Tseng, Ming-Daw Tsai and Shu-Chun Teng ()
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Zih-Jie Shen: College of Medicine, National Taiwan University
Pang-Hung Hsu: Genomics Research Center, Academia Sinica
Yu-Tai Su: College of Medicine, National Taiwan University
Chia-Wei Yang: College of Medicine, National Taiwan University
Li Kao: College of Medicine, National Taiwan University
Shun-Fu Tseng: College of Medicine, National Taiwan University
Ming-Daw Tsai: Genomics Research Center, Academia Sinica
Shu-Chun Teng: College of Medicine, National Taiwan University

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract In yeast, the initiation of telomere replication at the late S phase involves in combined actions of kinases on Cdc13, the telomere binding protein. Cdc13 recruits telomerase to telomeres through its interaction with Est1, a component of telomerase. However, how cells terminate the function of telomerase at G2/M is still elusive. Here we show that the protein phosphatase 2A (PP2A) subunit Pph22 and the yeast Aurora kinase homologue Ipl1 coordinately inhibit telomerase at G2/M by dephosphorylating and phosphorylating the telomerase recruitment domain of Cdc13, respectively. While Pph22 removes Tel1/Mec1-mediated Cdc13 phosphorylation to reduce Cdc13–Est1 interaction, Ipl1-dependent Cdc13 phosphorylation elicits dissociation of Est1–TLC1, the template RNA component of telomerase. Failure of these regulations prevents telomerase from departing telomeres, causing perturbed telomere lengthening and prolonged M phase. Together our results demonstrate that differential and additive actions of PP2A and Aurora on Cdc13 limit telomerase action by removing active telomerase from telomeres at G2/M phase.

Date: 2014
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DOI: 10.1038/ncomms6312

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